Purification and characterization of CEP from Lactococcus lactis ssp lactis

被引：11

作者：

Guo, Yuxing ^{[1
]}

Pan, Daodong ^{[1
]}

Zeng, Xiaoqun ^{[1
]}

Tanokura, Masaru ^{[2
]}

机构：

[1] Nanjing Normal Univ, Dept Food Sci & Nutr, Nanjing 210097, Peoples R China

[2] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo 1138657, Japan

来源：

FOOD CHEMISTRY | 2009年 / 112卷 / 03期

关键词：

CEP; Purification and characterization; Whey protein hydrolysate; ACE-inhibitory activity; ANGIOTENSIN-CONVERTING ENZYME; WALL-ASSOCIATED PROTEINASE; CELL-ENVELOPE PROTEINASE; PROTEOLYTIC-ENZYMES; SPECIFICITY; PEPTIDES; SEQUENCE;

D O I：

10.1016/j.foodchem.2008.06.002

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The cell-envelope proteinase (CEP) of Lactococcus lactis ssp. lactis LB12 was released from cells by treatment with lysozyme, purified by ammonium sulfate precipitation and chromatographed on DEAE-Sephadex A-25 and Sephacryl S-300 HR. The purified CEP is a monomer structure and has molecular mass of about 53 kDa. Optimal activity occurred at pH 7.5 and 40 degrees C. It is a metallopeptidase. activated by Mn2+, Mg2+, Ca2+, inhibited by Co2+, Zn2+, Ni2+ and EDTA, and a serine proteinase which is inhibited by PMSF. The sequence of the first 13 amino acids of the N-terminal of the CEP was determined to be Asp-Val-Phe-Ala-Pro-His-Met-Ala-Asn-Val-Ala-Ala-Val, and the whey protein hydrolysate produced by the CEP displayed ACE-inhibitory activity. (c) 2008 Elsevier Ltd. All rights reserved.

引用

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页码：533 / 538

页数：6

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